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Crystal structure of mouse ryanodine receptor 2 (residues 1-217)

Analyse Crystal structure of mouse ryanodine receptor 2 (residues 1-217) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3IM5
Type
protein
Length
348 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cardiac CA2+ release channel
UniProt
Q9ERN6
Pockets
3 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACardiac CA2+ release channelprotein1738% helix, 47% strandQ9ERN6
BCardiac CA2+ release channelprotein1758% helix, 45% strandQ9ERN6

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12540.640.8229empty
21650.460.7623empty
31120.420.7726empty

Interfaces

1 interface between chains.

  • A–B · 668 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3IM5 · Crystal structure of mouse Ryanodine Receptor 2 (residues 1-217) · the same entry in another collection · chain B against B, TM-score 1.00

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